MersV1, Main, Exploration, bibRecord, 004C62

Intermolecular localization of epitopes within an oligomeric protein by immunoelectron microscopy and image processing

Identifieur interne : 004C62 ( Main/Exploration ); précédent : 004C61; suivant : 004C63

Intermolecular localization of epitopes within an oligomeric protein by immunoelectron microscopy and image processing

Auteurs : Nicolas Boisset [France] ; Joachim Frank [États-Unis] ; Jean Christophe Taveau [France] ; Philippe Billiald [France] ; Genevieve Motta [France] ; Josette Lamy [France] ; Pierre Yves Sizaret [France] ; Jean Lamy [France]

Source :

Proteins: Structure, Function, and Bioinformatics [ 0887-3585 ] ; 1988.

RBID : ISTEX:4CC0865FB083372342E102B2BEE4CAB103C3DA93

Abstract

Three epitopes have been localized by immunoelectron microscopy on subunits Aa6 of the 4 × 6‐meric hemocyanin of the scorpion Androctonus australis. Soluble immunocomplexes composed of monoclonal antibodies and of native hemocyanin were purified, negatively stained with uranyle acetate by the single‐layer technique, and examined under the electron microscope (EM). The molecule images were digitized, aligned, and submitted to correspondence analysis according to the method of Van Heel and Frank (Ultramicroscopy 6: 187‐194, 1981). A high‐precision localization of the attachment point of the Fab arm to the antigen was achieved through a careful analysis of the average images. This method easily allowed the discrimination of epitopes located in different domains (Mr 20 kDa) of the same subunit. Nonoverlapping epitopes located in the same structural domain of subunit Aa6 could be distinguished by the stain exclusion patterns of their Fab arms. The method is general and may be used for epitope mapping in any antigen producing definite EM views.

Url:

https://api.istex.fr/ark:/67375/WNG-1WQ926X9-Z/fulltext.pdf

DOI: 10.1002/prot.340030305

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Three epitopes have been localized by immunoelectron microscopy on subunits Aa6 of the 4 × 6‐meric hemocyanin of the scorpion Androctonus australis. Soluble immunocomplexes composed of monoclonal antibodies and of native hemocyanin were purified, negatively stained with uranyle acetate by the single‐layer technique, and examined under the electron microscope (EM). The molecule images were digitized, aligned, and submitted to correspondence analysis according to the method of Van Heel and Frank (Ultramicroscopy 6: 187‐194, 1981). A high‐precision localization of the attachment point of the Fab arm to the antigen was achieved through a careful analysis of the average images. This method easily allowed the discrimination of epitopes located in different domains (Mr 20 kDa) of the same subunit. Nonoverlapping epitopes located in the same structural domain of subunit Aa6 could be distinguished by the stain exclusion patterns of their Fab arms. The method is general and may be used for epitope mapping in any antigen producing definite EM views.</div>
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Intermolecular localization of epitopes within an oligomeric protein by immunoelectron microscopy and image processing

Intermolecular localization of epitopes within an oligomeric protein by immunoelectron microscopy and image processing

Source :

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri